Structure of PDB 1kol Chain A

Receptor sequence
>1kolA (length=396) Species: 303 (Pseudomonas putida) [Search protein sequence]
GNRGVVYLGSGKVEVQKIDYPKMQDPRGKKIEHGVILKVVSTNICGSDQH
MVRGRTTAQVGLVLGHEITGEVIEKGRDVENLQIGDLVSVPFNVACGRCR
SCKEMHTGVCLTVNPARAGGAYGYVDMGDWTGGQAEYVLVPYADFNLLKL
PDRDKAMEKIRDLTCLSDILPTGYHGAVTAGVGPGSTVYVAGAGPVGLAA
AASARLLGAAVVIVGDLNPARLAHAKAQGFEIADLSLDTPLHEQIAALLG
EPEVDCAVDAVGFEARGHGHEGAKHEAPATVLNSLMQVTRVAGKIGIPGL
YVTEDPGAVDAAAKIGSLSIRFGLGWAKSHSFHTGQTPVMKYNRALMQAI
MWDRINIAEVVGVQVISLDDAPRGYGEFDAGVPKKFVIDPHKTFSA
3D structure
PDB1kol Crystal Structure of Formaldehyde Dehydrogenase from Pseudomonas putida: the Structural Origin of the Tightly Bound Cofactor in Nicotinoprotein Dehydrogenases
ChainA
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C46 G47 S48 H51 H67 E68 C97 C100 C103 C111 N115 D169 T173 K386
Catalytic site (residue number reindexed from 1) C45 G46 S47 H50 H66 E67 C96 C99 C102 C110 N114 D168 T172 K385
Enzyme Commision number 1.2.1.46: formaldehyde dehydrogenase.
1.2.98.1: formaldehyde dismutase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0018467 formaldehyde dehydrogenase (NAD+) activity
GO:0046872 metal ion binding
GO:0047895 formaldehyde dismutase activity

View graph for
Molecular Function
External links
PDB RCSB:1kol, PDBe:1kol, PDBj:1kol
PDBsum1kol
PubMed12445786
UniProtP46154|FADH_PSEPU Glutathione-independent formaldehyde dehydrogenase (Gene Name=fdhA)

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